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• W2155520512 abstract "Penicillin G amidase from Providencia rettgeri is a heterodimer of 92 kDa. We have previously expressed the Pr. rettgeri pac gene coding for this enzyme in Saccharomyces cerevisiae, and now we report the expression and characterization in the methylotrophic yeast Pichia pastoris. The recombinant catalytically active enzyme (rPAC(Pr)) was secreted from shake flask-grown P. pastoris cells into the medium at a level of approximately 0.18 U ml(-1). This yield of rPAC(Pr) was higher, by two orders of magnitude, than that obtained using a single-copy expression plasmid in S. cerevisiae. In addition, the secreted recombinant enzyme was entirely N-glycosylated. The recombinant PAC(Pr) was further characterized in terms of specific activity, kinetic parameters and thermostability. Except the significantly higher thermostability of the glycosylated rPAC(Pr) produced in P. pastoris, the other parameters were very similar to those of the corresponding non-glycosylated enzymes produced in bacteria or in S. cerevisiae. The higher thermostability of this recombinant enzyme has a clear industrial advantage." @default.
• W2155520512 created "2016-06-24" @default.
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• W2155520512 date "2002-01-01" @default.
• W2155520512 modified "2023-10-13" @default.
• W2155520512 title "Production of glycosylated thermostableProvidencia rettgeripenicillin G amidase inPichia pastoris" @default.
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• W2155520512 doi "https://doi.org/10.1111/j.1567-1364.2002.tb00045.x" @default.
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